There are four known laws of thermodynamics and the first one is the law of conservation of energy, which states that energy can neither be created nor destroyed. The quiz below covers how well you understand the different laws of thermodynamics and how to apply them in everyday life. All the best!
They consume energy to build up polymers from monomers.
They do not depend on enzymes.
They are usually highly spontaneous chemical reactions.
They release energy as they degrade polymers to monomers.
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Energy cannot be transferred or transformed.
The entropy of the universe is decreasing.
Kinetic energy is stored energy that results from the specific arrangement of matter.
The entropy of the universe is constant.
Energy cannot be created nor destroyed
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The organism ultimately must obtain all of the necessary energy for life from its environment.
Organisms are unable to transform energy.
The entropy of an organism decreases with time as the organism grows in complexity.
The energy content of an organism is constant.
Life does not obey the first law of thermodynamics.
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Life obeys the second law of thermodynamics because the decrease in entropy as the
Living organisms are able to transform energy into entropy.
As a consequence of growing, organisms create more disorder in their environment than the
Living organisms do not obey the second law of thermodynamics, which states that entropy
Living organisms do not follow the laws of thermodynamics.
Enthalpy of the universe
Free energy of the system
Free energy of the universe
Entropy of the universe
Entropy of the system
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Every chemical reaction must increase the total entropy of the universe.
If there is an increase in the energy of a system, there must be a corresponding decrease in the
Energy can be transferred or transformed, but it cannot be created or destroyed.
If the entropy of a system increases, there must be a corresponding decrease in the entropy of
Every energy transfer requires activation energy from the environment.
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Heat represents a form of energy that can be used by most organisms to do work.
Every energy transformation by a cell decreases the entropy of the universe.
Without an input of energy, organisms would tend toward decreasing entropy.
Cells require a constant input of energy to maintain their high level of organisation.
Conversion of energy from one form to another is always accompanied by some gain of free
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Hydrolysis
Respiration
Dehydation reaction
Catabolism
Digestion
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Requires that due to evolution, the entropy of the universe increased.
Is based on the fact that organisms function as closed systems.
Is consistent with the second law of thermodynamics.
A and B only
A, B and C
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A firefly using light flashes to attract a mate
Boy mowing grass
A food molecule made up of energy-rich macromolecules
Water rushing over Niagara Falls
An insect foraging for food
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A sealed terrarium
Food cooking in a pressure cooker
An organism
Liquid in a corked bottle
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Metabolism is a property of organismal life
Metabolism depends on an organism's adequate hydration
Metabolism manages the increase of entropy in an organism
Metabolism utilises all of an organism's resources
Metabolism depends on a constant supply of energy from food
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Slightly decreasing
Greatly increasing
Slightly increasing
Greatly decreasing
No change
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The reaction proceeds with a net release of free energy.
The products have more total energy than the reactants.
Some reactants will be converted to products.
The reactions are nonspontaneous.
A net input of energy from the surroundings is required for the reactions to proceed.
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A chemical reaction in which the entropy change in the reaction is just balanced by an
A reaction in which the free energy at equilibrium is higher than the energy content at any
An endergonic reaction in an active metabolic pathway where the energy for that reaction is
A chemical reaction in which both the reactants and products are only used in a metabolic
There is no possibility of having chemical equilibrium in any living cell.
Endothermic
Enthalpic
Spontaneous
Endergonic
Exothermic
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The system's entropy
The condition of a cell that is not able to react
The cell's energy equilibrium
The heat content of a chemical system
The total kinetic energy of a system
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It provides energy coupling between exergonic and endergonic reactions.
Its terminal phosphate group contains a strong covalent bond that when hydrolysed releases
Its terminal phosphate bond has higher energy than the other two.
Its hydrolysis provides an input of free energy for exergonic reactions.
All of the above are true.
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Reactant and product concentrations are not the same
Cells are open systems, but a test tube is a closed system.
The hydrolysis of ATP in a cell produces different chemical products than does the reaction in
The reaction in cells must be catalysed by enzymes, but the reaction in a test tube does not
Cells are less efficient at heat production than nonliving systems.
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A phosophilip
An RNA nucleotide
An amino acid with three phosphate groups
A DNA helix
An anabolic steroid
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Feedback regulation
Entropy
Bioenergetics
Cooperativity
Energy coupling
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They build up complex molecules such as protein from simpler compounds.
They combine molecules into more energy-rich molecules.
They are usually coupled with anabolic pathways to which they supply energy in the form of
They are endergonic.
They are spontaneous and do not need enzyme catalysis.
It is lost to the environment.
It is used to generate ADP from nucleotide precursors.
It is used to store energy as more ATP.
It is transported to specific organs such as the brain.
It is used to power yet more cellular work.
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It can be added to water and excreted as a liquid.
It can only be used to regenerate more ATP.
It can enter the nucleus to affect gene expression.
It can be added to other molecules in order to activate them.
It is released as an excretory waste.
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The nitrogen-containing base is different.
The number of phosphates is three instead of one.
The number of phosphates is three instead of two.
The sugar molecule is different.
There is no difference.
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The reaction always goes in the direction toward chemical equilibrium.
The reaction is faster than the same reaction in the absence of the enzyme.
The free energy change of the reaction is opposite from the reaction in the absence of the
A and B only
A, B and C
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Increase the entropy of the reactants.
Decrease the concentration of the reactants.
Cool the reactants.
Add a catalyst.
Increase the activation energy needed.
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Bringing glucose and fructose together to form sucrose.
Utilisation of water as a covalent bond is formed between glucose and fructose to form
Breaking the bond between glucose and fructose and forming new bonds from the atoms of
Production of water from the sugar as bonds are broken between the glucose monomers.
The release of water from sucrose as the bond between glucose and fructose is broken.
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Entropy
Activation energy
Endothermic level
Free-energy content
Heat content
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The hydrolysis of starch to sugar is endergonic.
The activation energy barrier for this reaction cannot be surmounted.
Starch cannot be hydrolysed in the presence of so much water.
Starch hydrolysis is nonspontaneous.
The starch solution has less free energy than the sugar solution.
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Enzymes are permanently altered by the reactions they catalyse.
Enzymes prevent changes in substrate concentrations.
Enzymes increase the rate of a reaction.
Enzymes change the direction of chemical reactions.
Enzymes decrease the free energy change of a reaction.
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+40 kcal/mol
-20 kcal/mol
+20 kcal/mol
0 kcal/mol
-40 kcal/mol
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Binds allosteric regulators of the enzyme.
Is inhibited by the presence of a coenzyme or a cofactor.
Is involved in the catalytic reaction of the enzyme.
Binds the products of the catalytic reaction.
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The binding of the substrate changes the shape of the enzyme's active site.
A competitive inhibitor can outcompete the substrate for the active site.
The active site creates a microenvironment ideal for the reaction.
The binding of the substrate depends on the shape of the active site.
Some enzymes change their structure when activators bind to the enzyme.
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Competitive inhibition
Denaturisation of the enzyme
Allosteric inhibition
Insufficient cofactors
Saturation of the enzyme activity
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Enzyme function is increased if the three-dimensional structure or conformation of an
Enzymes may require a nonprotein cofactor or ion for catalysis to take speed up more
Enzymes increase the rate of chemical reaction by lowering activation energy barriers.
Enzyme function is independent of physical and chemical environmental factors such as pH
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Cofactor necessary for enzyme activity.
Competitive inhibitor of the enzyme.
Coenzyme derived from a vitamin.
Noncompetitive inhibitor of the enzyme.
Allosteric activator of the enzyme.
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Succinate dehydrogenase is the enzyme, and malonic acid is the substrate.
Succinate is the substrate, and fumarate is the product.
Succinate dehydrogenase is the enzyme, and fumarate is the substrate.
Fumarate is the product, and malonic acid is a noncompetitive inhibitor.
Malonic acid is the product, and fumarate is a competitive inhibitor.
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It replaces the usual enzyme.
It blocks the binding of fumarate.
It is a competitive inhibitor.
It is able to bind to succinate.
It is a noncompetitive inhibitor.
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The hydrolysis of the ATP must be needed to allow the amino acid to bind to the synthetase.
The 3' end of the tRNA must have to be cleaved before it can have an attached amino acid.
The ATP must first have to attach to the tRNA.
The binding of the first two molecules must cause a 3-dimensional change that opens another
The tRNA molecule must have to alter its shape in order to be able to fit into the active site
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The enzyme forming covalent bonds with the reactants
The enzyme's ability to stretch reactants and move them toward a transition state
The ability of an enzyme to form a template for holding and joining molecules
The enzyme providing an appropriate microenvironment conducive to a reaction's occurrence
The enzyme becoming too saturated because of the concentration of substrate
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An increase in a cell's catabolic activity
An increased amino acid concentration
An increased influx of cofactor molecules
The cell's increased transport of materials to the environment
An increase in a cell's anabolic activity
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Change in the folding of enzymes
Removal of amine groups from your proteins
Binding of enzymes to inappropriate substrates
Destruction of your enzymes' primary structure
Removal of the amino acids in active sites
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By acting as a coenzyme for the reaction
By binding at the active site of the enzyme
By changing the free energy change of the reaction
By decreasing the activation energy of the reaction
By changing the shape of a reactant
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A coenzyme
A substrate
A product
An intermediate
An allosteric inhibitor
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The substrate
A coenzyme
A competitive inhibitor
An allosteric inhibitor
An imtermediate
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Metabolic inhibition
Noncooperative inhibition.
Reversible inhibition.
Feedback inhibition
Allosteric inhibition.
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A multi-enzyme complex contains all the enzymes of a metabolic pathway.
A product of a pathway serves as a competitive inhibitor of an early enzyme in the pathway.
A substrate molecule bound to an active site affects the active site of several subunits.
A substrate binds to an active site and inhibits cooperation between enzymes in a pathway.
Several substrate molecules can be catalysed by the same enzyme.
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